Chemical cross-linking with a diazirine photoactivatable cross-linker investigated by MALDI- and ESI-MS/MS

dc.creatorGomes, AF
dc.creatorGozzo, FC
dc.date2010
dc.dateAUG
dc.date2014-11-18T08:06:32Z
dc.date2015-11-26T17:48:03Z
dc.date2014-11-18T08:06:32Z
dc.date2015-11-26T17:48:03Z
dc.date.accessioned2018-03-29T00:30:50Z
dc.date.available2018-03-29T00:30:50Z
dc.identifierJournal Of Mass Spectrometry. John Wiley & Sons Ltd, v. 45, n. 8, n. 892, n. 899, 2010.
dc.identifier1076-5174
dc.identifierWOS:000281569100005
dc.identifier10.1002/jms.1776
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/63007
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/63007
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/63007
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1288972
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCrystallography and nuclear magnetic resonance are well-established methods to study protein tertiary structure and interactions. Despite their usefulness, such methods are not applicable to many protein systems. Chemical cross-linking of proteins coupled with mass spectrometry allows low-resolution characterization of proteins and protein complexes based on measuring distance constraints from cross-links. In this work, we have investigated cross-linking by means of a heterobifunctional cross-linker containing a traditional N-hydroxysuccinimide (NHS) ester and a UV photoactivatable diazirine group. Activation of the diazirine group yields a highly reactive carbene species, with potential to increase the number of cross-links compared with homobifunctional, NHS-based cross-linkers. Cross-linking reactions were performed on model systems such as synthetic peptides and equine myoglobin. After reduction of the disulfide bond, the formation of intra- and intermolecular cross-links was identified and the peptides modified with both NHS and diazirine moieties characterized. Fragmentation of these modified peptides reveals the presence of a marker ion for intramolecular cross-links, which facilitates identification. Copyright (c) 2010 John Wiley & Sons, Ltd.
dc.description45
dc.description8
dc.description892
dc.description899
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [FAPESP 2004/14846-0, FINEP 01 07 0290.00]
dc.descriptionFAPESP [FAPESP 08/57805-2, CNPq 573672/2008-3]
dc.languageen
dc.publisherJohn Wiley & Sons Ltd
dc.publisherChichester
dc.publisherInglaterra
dc.relationJournal Of Mass Spectrometry
dc.relationJ. Mass Spectrom.
dc.rightsfechado
dc.rightshttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.sourceWeb of Science
dc.subjectcross-linking
dc.subjectmass spectrometry, diazirine
dc.subjectfragmentation
dc.subjectphotoactivatable
dc.subjectApolipoprotein-a-i
dc.subjectMass-spectrometry
dc.subject3-dimensional Structure
dc.subjectProtein Structures
dc.subjectPeptides
dc.subjectProximity
dc.subjectIdentification
dc.subjectBenzophenone
dc.subjectBiochemistry
dc.subjectConstraints
dc.titleChemical cross-linking with a diazirine photoactivatable cross-linker investigated by MALDI- and ESI-MS/MS
dc.typeArtículos de revistas


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